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Mudi Sheves
Home Page of Prof. Mordechai (Mudi) Sheves
Vice President for Technology Transfer, Weizmann Institute of Science

The Ephraim Katzir/Rao Makineni Professorial Chair of Chemistry

The Weizmann Institute of Science
76100 Rehovot, Israel
telephone: +972 (8) 934-4320 

Members of the group:

Dr. Noga Friedman
Yamit Shaarabi
Dr. Tamar Eliash
Elena Smolensky
Dr. Tushar Kanti Maiti
Consultant: Dr. Amiram Hirshfeld

Ph.D., Postdoctoral positions available!

Research in our Group

Molecular Mechanism for the Function of Retinal Proteins

Biological activity of visual pigments and bacteriorhodopsin is related to a photocycle during which both the retinal and the opsin moieties undergo a series of structural changes. The molecular changes and their correlation with the corresponding biological functions (i.e., the release of the diffusable transmitter in visual pigments and the pumping of H+ ions in bacteriorhodopsin) is of primary importance. Clarifying these functions may be achieved by obtaining a structural description of the polyene chromophore, its spectroscopic properties at the binding site, its opsin environment, and the changes occurring in retinal-opsin interactions following light absorption. Using artificial pigments, model compounds in solution and spectroscopic methods (absorption, FTIR, NMR and AFM), we have shed light on the role that single and double bonds play in the photocycle, protein-chromophore interactions in the binding site and the role of water and light in retinal protein activity.

List of all publications (including DOIs) [Submit additions and corrections]

Selected publications

Vogel, R; Ludeke, S; Radu, I; Siebert, F; Sheves, M. Photoreactions of metarhodopsin III. Biochemistry 43 (31): 10255-10264 (2004). [Read online]

Vogel, R; Siebert, F; Zhang, XY; Fan, GB; Sheves, M. Formation of meta III during the decay of activated rhodopsin proceeds via meta I and not via meta II. Biochemistry 43 (29): 9457-9466 (2004). [Read online]

Friedman, N; Ottolenghi, M; Sheves, M. Heterogeneity effects in the binding of all-trans retinal to bacterio-opsin. Biochemistry 42 (38): 11281-11288 (2003). [Read online]

A. Aharoni, A. Khatchatouriants, A. Manevitch, A. Lewis, and M. Sheves, Protein-beta-ionone ring interactions enhance the light-induced dipole of the chromophore in bacteriorhodopsin J. Phys. Chem. B 107, 6221-6225 (2003) [read online]

U. Zadok, A. Khatchatouriants, A. Lewis, et al. Light-induced charge redistribution in the retinal chromophore is required for initiating the bacteriorhodopsin photocycle J. Am. Chem. Soc. 124, 11844-11845 (2002) [read online]

A. Aharoni, M. Ottolenghi and M. Sheves, Light induced hydrolysis and rebinding of non-isomerizable bacteriorhodopsin pigment, Biophys. J. 82,2617 (2002). [Read online]

A. Aharoni, L. Weiner, A. Lewis, M.Ottolenghi and M. Sheves. Retinal chromophores initiate light-induced conformational alterations in bacterio-opsin. J. Am. Chem. Soc. 123, 6612 (2001). [Read online]

A. Aharoni, L. Weiner, M. Ottolenghi and M. Sheves. Bacteriorhodopsin experiences light-induced conformational alterations in non-isomerizable C13=C14 pigments. A study with EPR. J. Biol. Chem. 275, 21010 (2000).[read online]

I. Rousso, Y. Gat, A. Lewis, M. Sheves and M. Ottolenghi. Effective light-induced hydroxylamine reactions occur with C13=C14 non-isomerizable pigments. Biophys. J. 75, 413 (1998) [read online]

I. Rousso, E. Khachatryan, Y. Gat, I. Brodsky, M. Ottolenghi, M. Sheves and A. Lewis. Light-driven protein conformational changes in bacteriorhodopsin are triggered by an induced retinal dipole. Proc. Natl. Acad. Sci. USA. 94, 7937 (1997).[read online]

I. Rousso, M. Sheves and A. Lewis. Protein structure alteration induced by light activated water adsorption. A study with bacteriorhodopsin. J. Am. Chem. Soc. 118, 11299 (1996).[read online]

A. Lewis, I. Rousso, E. Khachatryan, I. Brodsky and M. Sheves. Directly probing rapid membrane protein dynamics with an atomic force microscope. Biophys. J. 70, 2380 (1996).[read abstract]

J. Delaney, T. Brack, G. Atkinson, M. Ottolenghi, G. Steinberg and M. Sheves. Primary picosecond molecular events in the photoreaction of the bR5.12 artificial bacteriorhodopsin pigment. Proc. Natl. Acad. Sci. USA 92, 2101 (1995).[read online]

S. Druckmann, M. Ottolenghi, I. Rousso, N. Friedman and M. Sheves, Time resolved titrations of the Schiff base and of the Asp-85 residue in artificial bacteriorhodopsins. Biochemistry 34, 12066 (1995).

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